The intracellular pathway of vitellogenin secretion in the frog hepatocyte as revealed by protein A-gold immunocytochemistry.

Herbener, George H.; Bendayan, Moı̈se; Feldhoff, Richard C.

doi:10.1177/32.7.6610700

Cited by 25 publications

(11 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the studies of albumin and vitellogenin secretion by frog hepatocyte (Herbener et al, 1984(Herbener et al, ,1986 (Figs. 26 and 27), the quantitative evaluations demonstrated changes in the cellular processing of these secretory proteins under experimental conditions.…”

Section: A P P L I C a T I O N O F T H E P R O T E I N A -G O L D A Nmentioning

confidence: 99%

Protein A–Gold and Protein G–Gold Postembedding Immunoelectron Microscopy

Bendayan¹

1989

Colloidal Gold

View full text Add to dashboard Cite

Section: A P P L I C a T I O N O F T H E P R O T E I N A -G O L D A Nmentioning

confidence: 99%

Protein A–Gold and Protein G–Gold Postembedding Immunoelectron Microscopy

Bendayan¹

1989

Colloidal Gold

View full text Add to dashboard Cite

“…The VTG-colloidal gold complex was formed according to Herbener e/al. [19] and De Mey [10]. Before complexing, VTG was diluted to 0.5 mg/ml and the concentration of the buffer not exceeding 7 raM, pH 7.5.…”

Section: Preparation Of Colloidal Gold Conjugated Vtgmentioning

confidence: 99%

Pathway and kinetics of vitellogenin‐gold internalization in the Xenopus oocyte

Busson

Ovtracht

Gounon

1989

Biology of the Cell

View full text Add to dashboard Cite

After in vitro incubation of Xenopus oocytes with vitellogenin (VTG)-gold conjugate, the gold particles are distributed on the whole plasma membrane. Their concentration in coated pits still occurs at 0 degrees C. At +20 degrees C the label quickly (30 sec) appears in multi-vesicular endosomes (MVE) which segregate together with primary endocytic vesicles into distinct clusters below the plasma membrane. From this step up to crystallization of the yolk platelets, the gold particles stay in the same compartment. During 5.5 h the label progressively increases along the MVE membrane, first (1.5 h) by fusion of primary endocytic vesicles with consecutively enlarging endosomes, then (4 h) by decreasing of the MVE membrane. As concerns the yolk platelet formation, concentration of primordial yolk platelets (PYP) occurs at 5.5 h from the incubation onset, the labeling of preexisting yolk platelets starts at 7 h, while crystallization of PYP begins only after 12-13 h. Our results indicate that VTG receptors are not preclustered in coated pits and their lateral translation is not inhibited at 0 degrees C. The yolk protein processing takes place within one compartment only. The VTG condensation begins with a long concentration phase of receptor-VTG complexes still integrated in the endosome membrane. It occurs in MVE by: i) a repeated fusion of primary endocytic vesicles; ii) removing part of the endosome membrane by internal vesiculation. Fusion between endosomes occurs only after VTG has dissociated from its receptors and VTG dissociates only when when the density of the VTG-receptor complexes in the endosome membrane is sufficient. Crystallization begins after a 7-8 h delay. The endosome migration into the oocyte is also controlled by the binding of VTG to its receptors. Our results also demonstrate that binding of VTG colloidal gold modifies neither the vitellogenic pathway nor the duration of the vitellogenin internalization. However when vitellogenin is bound to colloidal gold, dissociation of ligand-receptor complexes is delayed because the amount of ligand in the incubation medium is necessarily low.

show abstract

“…Vg is thus a liver-specific protein in vertebrate females. Immunohistochemical localization of Vg has been reported for fish (Prisco et al 2002;Kobayashi et al 2005), amphibians (Herbener et al 1984), reptiles (Tada et al 2004), and birds (Wachsmuth & Jost 1976), in which Vg is detected in the liver and ovary of female organisms without exception (Roubal et al 1997;Van der Ven et al 2003;Desantis et al 2005). However, information concerning the localization of Vg in invertebrate organisms is relatively limited.…”

mentioning

confidence: 99%

Immunohistochemical localization of vitellogenin in the hepatic diverticulum of the amphioxus Branchiostoma belcheri tsingtauense, with implications for the origin of the liver

Han

Zhang

Wang

et al. 2006

Invertebrate Biology

View full text Add to dashboard Cite

Abstract. The localization of vitellogenin (Vg) remains untested in amphioxus. Western blotting analysis showed that mouse anti‐amphioxus Vg sera cross‐reacted with the crude extracts of the hepatic diverticulum and ovary, and humoral fluids, including blood and coelomic fluid, from specimens of Branchiostoma belcheri. Similarly, immunohistochemical staining also revealed that Vg is localized in the hepatic diverticulum, sub‐intestinal vessels, and ovary in amphioxus. The hepatic diverticulum of amphioxus, like the vertebrate liver, synthesizes Vg, suggesting that amphioxus hepatic diverticulum is functionally equivalent to the vertebrate liver in respect of the synthesis of this compound. This agrees with the idea that amphioxus hepatic diverticulum is the precursor of vertebrate liver.

show abstract

The intracellular pathway of vitellogenin secretion in the frog hepatocyte as revealed by protein A-gold immunocytochemistry.

Cited by 25 publications

References 7 publications

Protein A–Gold and Protein G–Gold Postembedding Immunoelectron Microscopy

Protein A–Gold and Protein G–Gold Postembedding Immunoelectron Microscopy

Pathway and kinetics of vitellogenin‐gold internalization in the Xenopus oocyte

Immunohistochemical localization of vitellogenin in the hepatic diverticulum of the amphioxus Branchiostoma belcheri tsingtauense, with implications for the origin of the liver

Contact Info

Product

Resources

About